Virus-encoded aminoacyl-tRNA synthetases: structural and functional characterization of mimivirus TyrRS and MetRS
- PMID: 17855524
- PMCID: PMC2169003
- DOI: 10.1128/JVI.01107-07
Virus-encoded aminoacyl-tRNA synthetases: structural and functional characterization of mimivirus TyrRS and MetRS
Abstract
Aminoacyl-tRNA synthetases are pivotal in determining how the genetic code is translated in amino acids and in providing the substrate for protein synthesis. As such, they fulfill a key role in a process universally conserved in all cellular organisms from their most complex to their most reduced parasitic forms. In contrast, even complex viruses were not found to encode much translation machinery, with the exception of isolated components such as tRNAs. In this context, the discovery of four aminoacyl-tRNA synthetases encoded in the genome of mimivirus together with a full set of translation initiation, elongation, and termination factors appeared to blur what was once a clear frontier between the cellular and viral world. Functional studies of two mimivirus tRNA synthetases confirmed the MetRS specificity for methionine and the TyrRS specificity for tyrosine and conformity with the identity rules for tRNA(Tyr) for archea/eukarya. The atomic structure of the mimivirus tyrosyl-tRNA synthetase in complex with tyrosinol exhibits the typical fold and active-site organization of archaeal-type TyrRS. However, the viral enzyme presents a unique dimeric conformation and significant differences in its anticodon binding site. The present work suggests that mimivirus aminoacyl-tRNA synthetases function as regular translation enzymes in infected amoebas. Their phylogenetic classification does not suggest that they have been acquired recently by horizontal gene transfer from a cellular host but rather militates in favor of an intricate evolutionary relationship between large DNA viruses and ancestral eukaryotes.
Figures
Similar articles
-
Structural basis for orthogonal tRNA specificities of tyrosyl-tRNA synthetases for genetic code expansion.Nat Struct Biol. 2003 Jun;10(6):425-32. doi: 10.1038/nsb934. Nat Struct Biol. 2003. PMID: 12754495
-
Distant Mimivirus relative with a larger genome highlights the fundamental features of Megaviridae.Proc Natl Acad Sci U S A. 2011 Oct 18;108(42):17486-91. doi: 10.1073/pnas.1110889108. Epub 2011 Oct 10. Proc Natl Acad Sci U S A. 2011. PMID: 21987820 Free PMC article.
-
Studies on crenarchaeal tyrosylation accuracy with mutational analyses of tyrosyl-tRNA synthetase and tyrosine tRNA from Aeropyrum pernix.J Biochem. 2012 Dec;152(6):539-48. doi: 10.1093/jb/mvs114. Epub 2012 Sep 29. J Biochem. 2012. PMID: 23024156
-
Discrimination between transfer-RNAs by tyrosyl-tRNA synthetase.Biochimie. 1993;75(12):1099-108. doi: 10.1016/0300-9084(93)90009-h. Biochimie. 1993. PMID: 8199245 Review.
-
Evolution of the tRNA(Tyr)/TyrRS aminoacylation systems.Biochimie. 2005 Sep-Oct;87(9-10):873-83. doi: 10.1016/j.biochi.2005.03.008. Epub 2005 Apr 8. Biochimie. 2005. PMID: 16164994 Review.
Cited by
-
Functional redundancy revealed by the deletion of the mimivirus GMC-oxidoreductase genes.Microlife. 2024 Apr 5;5:uqae006. doi: 10.1093/femsml/uqae006. eCollection 2024. Microlife. 2024. PMID: 38659623 Free PMC article.
-
Aminoacyl-tRNA synthetase interactions in SARS-CoV-2 infection.Biochem Soc Trans. 2023 Dec 20;51(6):2127-2141. doi: 10.1042/BST20230527. Biochem Soc Trans. 2023. PMID: 38108455 Free PMC article. Review.
-
Kratosvirus quantuckense: the history and novelty of an algal bloom disrupting virus and a model for giant virus research.Front Microbiol. 2023 Nov 30;14:1284617. doi: 10.3389/fmicb.2023.1284617. eCollection 2023. Front Microbiol. 2023. PMID: 38098665 Free PMC article. Review.
-
Virologs, viral mimicry, and virocell metabolism: the expanding scale of cellular functions encoded in the complex genomes of giant viruses.FEMS Microbiol Rev. 2023 Sep 5;47(5):fuad053. doi: 10.1093/femsre/fuad053. FEMS Microbiol Rev. 2023. PMID: 37740576 Free PMC article.
-
Giant viruses of the Megavirinae subfamily possess biosynthetic pathways to produce rare bacterial-like sugars in a clade-specific manner.Microlife. 2022 Apr 6;3:uqac002. doi: 10.1093/femsml/uqac002. eCollection 2022. Microlife. 2022. PMID: 37223350 Free PMC article.
References
-
- Abergel, C., B. Coutard, D. Byrne, S. Chenivesse, J. B. Claude, C. Deregnaucourt, T. Fricaux, C. Gianesini-Boutreux, S. Jeudy, R. Lebrun, C. Maza, C. Notredame, O. Poirot, K. Suhre, M. Varagnol, and J.-M. Claverie. 2003. Structural genomics of highly conserved microbial genes of unknown function in search of new antibacterial targets. J. Struct. Funct. Genomics 4:141-157. - PubMed
-
- Adl, S. M., A. G. Simpson, M. A. Farmer, R. A. Andersen, O. R. Anderson, J. R. Barta, S. S. Bowser, G. Brugerolle, R. A. Fensome, S. Fredericq, T. Y. James, S. Karpov, P. Kugrens, J. Krug, C. E. Lane, L. A. Lewis, J. Lodge, D. H. Lynn, D. G. Mann, R. M. McCourt, L. Mendoza, O. Moestrup, S. E. Mozley-Standridge, T. A. Nerad, C. A. Shearer, A. V. Smirnov, F. W. Spiegel, and M. F. Taylor. 2005. The new higher level classification of eukaryotes with emphasis on the taxonomy of protists. J. Eukaryot. Microbiol. 52:399-451. - PubMed
-
- Arnez, J. G., and D. Moras. 1997. Structural and functional considerations of the aminoacylation reaction. Trends Biochem. Sci. 22:211-216. - PubMed
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Molecular Biology Databases
Research Materials